负责凝血酶对多形核白细胞趋化特性的结构域的定位。

Localization of the structural domain responsible for the chemotactic properties of thrombin on polymorphonuclear leukocytes.

作者信息

Morin A, Arvier M M, Doutremepuich F, Vigneron C

机构信息

Centre de Transfusion sanguine, Vandoeuvre, France.

出版信息

Thromb Res. 1990 Oct 1;60(1):33-42. doi: 10.1016/0049-3848(90)90337-c.

DOI:10.1016/0049-3848(90)90337-c

PMID:2278036

Abstract

Human alpha thrombin at 1.1.10(-5) M is chemotactic for human polymorphonuclear leukocytes. This thrombin property disappears when the alpha thrombin (1.1.10(-5) M) hirudin (1.32.10(-5) M) mixture is realized. The same result is obtained when the thrombin at 1.1. 10(-5) M is inhibited by antithrombin III in a ratio of 1 mol of thrombin for 4.5 mol of antithrombin III. The hirudin and the antithrombin III appear therefore to mask, by their binding the structural domain responsible for the chemotactic properties of thrombin on polymorphonuclear leukocytes.

摘要

1.1×10⁻⁵ M 的人α凝血酶对人多形核白细胞具有趋化作用。当实现α凝血酶（1.1×10⁻⁵ M）与水蛭素（1.32×10⁻⁵ M）的混合时，这种凝血酶特性消失。当1.1×10⁻⁵ M 的凝血酶被抗凝血酶III以1摩尔凝血酶对4.5摩尔抗凝血酶III的比例抑制时，也会得到相同的结果。因此，水蛭素和抗凝血酶III似乎通过它们的结合掩盖了负责凝血酶对多形核白细胞趋化特性的结构域。